Insight into cyanobacterial circadian timing from structural details of the KaiB-KaiC interaction.

@article{Snijder2014InsightIC,
  title={Insight into cyanobacterial circadian timing from structural details of the KaiB-KaiC interaction.},
  author={Joost Snijder and Rebecca J. Burnley and Anika Wiegard and Adrien S. J. Melquiond and Alexandre M. J. J. Bonvin and Ilka M. Axmann and Albert J. R. Heck},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 4},
  pages={
          1379-84
        }
}
Circadian timing in cyanobacteria is determined by the Kai system consisting of KaiA, KaiB, and KaiC. Interactions between Kai proteins change the phosphorylation status of KaiC, defining the phase of circadian timing. The KaiC-KaiB interaction is crucial for the circadian rhythm to enter the dephosphorylation phase but it is not well understood. Using mass spectrometry to characterize Kai complexes, we found that KaiB forms monomers, dimers, and tetramers. The monomer is the unit that… CONTINUE READING

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